Detail Information for IndEnz0010001756
IED ID IndEnz0010001756
Enzyme Type ID esterase001756
Protein Name Serum paraoxonase/arylesterase 1
PON 1
EC 3.1.1.2
EC 3.1.1.81
EC 3.1.8.1
Aromatic esterase 1
A-esterase 1
Serum aryldialkylphosphatase 1
Gene Name Pon1 Pon
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAKLLALTLVGLVLALYKNHRSSYQTRLNAFREVTPVELPNCNLVKGIETGAEDLEILPNGLTFFSTGLKYPGIKSFDPSKPGKILLMDLNKKEPAVSELEIIGNTLDISSFNPHGISTFTDEDNTVYLLVVNHPDSSSTVEVFKFQEEERSLLHLKTITHELLPSINDIAAIGPESFYATNDHYFADPYLRSWEMYLGLSWSNVVYYSPDKVQVVAEGFDFANGIGISLDGKYVYIAELLAHKIHVYEKHANWTLTPLKVLNFDTLVDNISVDPVTGDLWVGCHPNGMRIFFYDAENPPGSEVLRIQNILSEDPKITVVYAENGTVLQGTTVASVYKGKLLIGTVFHKALYCDL
Enzyme Length 355
Uniprot Accession Number P52430
Absorption
Active Site ACT_SITE 115; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P27169
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence={ECO:0000269|PubMed:15963993}; CATALYTIC ACTIVITY: Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:15963993}; CATALYTIC ACTIVITY: Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81; Evidence={ECO:0000269|PubMed:15963993};
DNA Binding
EC Number 3.1.1.2; 3.1.1.81; 3.1.8.1
Enzyme Function FUNCTION: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification. {ECO:0000250|UniProtKB:P27169}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (8); Sequence conflict (2); Signal peptide (1)
Keywords Calcium;Disulfide bond;Glycoprotein;HDL;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space.
Modified Residue
Post Translational Modification PTM: The signal sequence is not cleaved. {ECO:0000250|UniProtKB:P27169}.
Signal Peptide SIGNAL 1..?; /note=Not cleaved
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10393212; 10748217; 11798161; 11893784; 12135950; 12466851; 12633754; 12654470; 12840045; 14681479; 14703510; 15213869; 15388641; 15721011; 15977192; 16260097; 16284190; 16341224; 16407304; 16602821; 16615898; 16682028; 17122353; 17717299; 18356571; 18358245; 18402813; 18597495; 18678600; 18757308; 18762170; 19034653; 19082953; 19371602; 19474728; 19556304; 20149374; 20189567; 20221870; 20221873; 20221875; 20221879; 20931267; 21044894; 21267068; 21530644; 21673326; 21677750; 21862013; 22001906; 22096492; 22406444; 22653878; 22916088; 23207871; 23405202; 23448543; 23582715; 23620511; 23639858; 23772025; 23908111; 24844689; 24971380; 25028362; 25069821; 25070982; 25230879; 25958017; 26176406; 26993251; 27010443; 28657647; 30389914; 30572120; 30905786; 32976529; 33838286; 8661009; 8811508; 8812495; 8825627; 8827514; 9176667; 9457688; 9475163; 9685159; 9745924;
Motif
Gene Encoded By
Mass 39,565
Kinetics
Metal Binding METAL 53; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169; METAL 54; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P27169; METAL 117; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P27169; METAL 168; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169; METAL 169; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P27169; METAL 224; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169; METAL 269; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169; METAL 270; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169
Rhea ID RHEA:17309; RHEA:22576
Cross Reference Brenda 3.1.1.2;3.1.1.25;3.1.8.1;